In situ and in vitro kinetics of phenol hydroxylase.


The half saturation constant for phenol was much lower with phenol hydroxylase in situ than with the purified enzyme, whereas the constant for NADPH was higher. In both cases, the linearized plots of the Michaelis-Menten equation were biphasic and the half saturation constants for all phenolic substrates were several times lower, when the phenol was added… (More)


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@article{Mrtberg1987InSA, title={In situ and in vitro kinetics of phenol hydroxylase.}, author={M M{\"o}rtberg and Halina Y. Neujahr}, journal={Biochemical and biophysical research communications}, year={1987}, volume={146 1}, pages={41-6} }